MolNFT v1 · #41315 · protein
Structure of closed cytochrome P450 eryk
2JJN · Cytochrome P450 113A1: “Structure of closed cytochrome P450 eryk”. X-ray diffraction, 2 ligands (HEM, SO4), 2 pockets (best druggability 0.86). MolNFT v1 #41315 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2JJN
- Type
- protein
- Length
- 395 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 113A1
- EC
- 1.14.-.-
- UniProt
- P48635
- Ligands
- HEM, SO4
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 113A1 (EC 1.14.-.-) | protein | 395 | 50% helix, 9% strand | P48635 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1147 | 0.86 | 0.87 | 101 | HEM |
| 2 | 110 | 0.44 | 0.78 | 24 | SO4 |
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P48635
- Elsewhere: RCSB PDB 2JJN · PDBe 2JJN · UniProt P48635
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